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Information on EC 4.2.3.15 - myrcene synthase
for references in articles please use BRENDA:EC4.2.3.15
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IUBMB Comments
A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
The enzyme appears in viruses and cellular organisms
showSynonyms
tps10, myrcene synthase, aatps2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 4.1.99.9
-
-
formerly
-
myrcene synthase
additional information
see also EC 4.2.3.83, EC 4.2.3.81, and EC 4.2.3.82
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = myrcene + diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination, C-O bond cleavage
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
ipsdienol biosynthesis, monoterpene biosynthesis, oleoresin monoterpene volatiles biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase (myrcene-forming)
A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
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CAS REGISTRY NUMBER
COMMENTARY
197462-59-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
(+)-limonene + diphosphate
Substrates: -
Products: less than 5% of total hydrocarbon product
Products: less than 5% of total hydrocarbon product
?
geranyl diphosphate
(-)-limonene + diphosphate
Substrates: -
Products: less than 5% of total hydrocarbon product
Products: less than 5% of total hydrocarbon product
?
geranyl diphosphate
(E)-beta-ocimene + diphosphate
Substrates: -
Products: 20% of total hydrocarbon product
Products: 20% of total hydrocarbon product
?
geranyl diphosphate
2-carene + diphosphate
Substrates: -
Products: less than 5% of total hydrocarbon product
Products: less than 5% of total hydrocarbon product
?
geranyl diphosphate
beta-myrcene + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + sabinene + linalool + limonene + diphosphate
-
Substrates: -
Products: formation of 53.8% myrcene, 20.9% sabinene, 19.8% linalool and 5.5% limonene
Products: formation of 53.8% myrcene, 20.9% sabinene, 19.8% linalool and 5.5% limonene
?
geranyl diphosphate
tricyclene + diphosphate
Substrates: -
Products: less than 5% of total hydrocarbon product
Products: less than 5% of total hydrocarbon product
?
linalyl diphosphate
acyclic and cyclic monoterpenes
-
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: induced by stem wounding, enhances resistance to insects
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: -
Products: 56% of total hydrocarbon product
Products: 56% of total hydrocarbon product
?
geranyl diphosphate
myrcene + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: -
Products: products of Arabidopsis thaliana TPS10 are 56% beta-myrcene, 20% (E)-beta-ocimene, and less than 5% each of (+)-limonene, (-)-limonene, 2-carene, and tricyclene and an unknown monoterpene
Products: products of Arabidopsis thaliana TPS10 are 56% beta-myrcene, 20% (E)-beta-ocimene, and less than 5% each of (+)-limonene, (-)-limonene, 2-carene, and tricyclene and an unknown monoterpene
?
geranyl diphosphate
myrcene + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: the acyclic monoterpene myrcene is required for the production of the major aggregation pheromone component, ipsdienol
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: bifunctional enzyme: geranyldiphosphate synthase (EC 2.5.1.1)/myrcene synthase (EC 4.2.3.15). When the recombinant enzyme is incubated with dimethylallyl diphosphate and isopentenyl diphosphate as cosubstrates, the level of geranyl diphosphate formed is approximately tenfold higher than the level of myrcene formed. The data suggest that geranyl diphosphate is a free intermediate in myrcene production
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: terpenes produced from the wild-type and mutant enzymes are identical, showing low levels of beta-myrcene from AcTPS2-K514A
Products: -
Products: -
?
additional information
?
-
Substrates: GC-MS analysis and identification of products from enzyme catalysis. Enzyme AaTPS2 produces a single product, beta-myrcene. No activity with farnesyl diphosphate or geranylgeranyl diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: GC-MS analysis and identification of products from enzyme catalysis. Enzyme AaTPS2 produces a single product, beta-myrcene. No activity with farnesyl diphosphate or geranylgeranyl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: GC-MS analysis of compounds. Wild-type CiCaMS hardly produces sesquiterpenes when farnesyl diphosphate (FDP) is supplied as a substrate
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
beta-myrcene + diphosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: terpenes produced from the wild-type and mutant enzymes are identical, showing low levels of beta-myrcene from AcTPS2-K514A
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: induced by stem wounding, enhances resistance to insects
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: -
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
Substrates: the acyclic monoterpene myrcene is required for the production of the major aggregation pheromone component, ipsdienol
Products: -
Products: -
?
geranyl diphosphate
myrcene + diphosphate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
-
sequence contains conserved sequences R28(R)X8W and D321DXXD encoing putative Mg2+-binding sites
additional information
-
wild-type AcTPS2 is significantly more active when KCl is absent from the activity buffer
additional information
although both Mg2+ and Mn2+ are able to support the catalytic activity of enzyme AaTPS2, an altered product spectrum is observed in the presence of Mn2+ for AaTPS2
additional information
-
although both Mg2+ and Mn2+ are able to support the catalytic activity of enzyme AaTPS2, an altered product spectrum is observed in the presence of Mn2+ for AaTPS2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme: geranyldiphosphate synthase/myrcene synthase
SwissProt
brenda
the tandem arginine motif RRX8W is conserved in the deduced protein of TPS10; bifunctional myrcene/(E)-beta-ocimene synthase
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression correlates well with floral volatile organic compounds emission in scented Alstroemeria genotypes
brenda
additional information
additional information
quantitative RT-PCR expression analysis in plants tissues. AaTPS2 exhibits the highest expression level in stem, and low expression in the other tissues
brenda
additional information
-
quantitative RT-PCR expression analysis in plants tissues. AaTPS2 exhibits the highest expression level in stem, and low expression in the other tissues
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
in Artemisia annua, three monoterpene synthases AaTPS2, AaTPS5, and AaTPS6, produce beta-myrcene, camphene, and 1,8-cineole as the major products, respectively, analysis of monoterpenes and sesquiterpenes produced by Artemisia annua plants, overview
physiological function
-
a whole cell myrcene-sensing biosensor is established that is based on the MyrR regulator from Pseudomonas sp.. The dynamic range is optimized by changing the cognate promoter. The biosensor is highly specific, rapid, user-friendly and low-cost in MS directed evolution comparing with other HTS methods. The constructed biosensor was applied for myrcene synthase directed evolution resulting in improving the activity of myrcene synthase
evolution
the enzyme AaTPS2 belongs to the TPS superfamily, subclade TPS-b
evolution
two TPSs from the Camphor tree Cinnamomum camphora are analyzed, one of these, CiCaMS, acts as a monoterpene synthase (monoTPS), and mediates the production of myrcene (EC 4.2.3.15), while the other, CiCaSSy, acts as a sesquiterpene synthase (sesquiTPS), and catalyses the production of alpha-santalene (EC 4.2.3.82), beta-santalene (EC 4.2.3.83), and trans-alpha-bergamotene (EC 4.2.3.81). These enzymes share 97% DNA sequence identity and differ only in 22 amino acid residues out of 553. To understand which residues are essential for the catalysis of monoterpenes resp. sesquiterpenes, a number of hybrid synthases are prepared, and supplemented by a set of single-residue variants. These are tested for their ability to produce monoterpenes and sesquiterpenes by in vivo production of sesquiterpenes in transgenic Escherichia coli, and by in vitro enzyme assays. Three residues in the sequence can mediate the change in product specificity from a monoterpene synthase to a sesquiterpene synthase. Another set of three residues defines the sesquiterpene product profile, including the ratios between sesquiterpene products
Show AA Sequence and Transmembrane Helices (103 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72500
calculated MW of recombinant protein expressed in Escherichia coli
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K514A
-
AcTPS2 mutant, 90% reduction in monoterpene synthase activity compared to wild-type enzyme
K514S
-
AcTPS2 mutant, presence of Ser is not able to rescue any of the activity lost after the removal of the Lys residue
A419E
site-directed mutagenesis, the mutation does not confer sesquiterpene synthase activity on CiCaMS
E308D
site-directed mutagenesis, no major change in monoterpene production is observed
F294M
site-directed mutagenesis, the active site mutant shows low but well detectable production of trans-alpha-bergamotene
G273A
site-directed mutagenesis, no major change in monoterpene production is observed
H415Q
site-directed mutagenesis, the mutation does not confer sesquiterpene synthase activity on CiCaMS
L291I
site-directed mutagenesis, active site mutant, no major change in monoterpene production is observed
L403F
site-directed mutagenesis, the mutant shows production of trans-alpha-bergamotene
L404V
site-directed mutagenesis, the mutant shows production of trans-alpha-bergamotene
S267N
site-directed mutagenesis, active site mutant, major change in monoterpene production is observed
additional information
additional information
the N-terminal signal peptide of AaTPS2 (46 amino acid residues) before RR motif is truncated and recombinantly expressed in Escherichia coli strain BL21(DE3)
additional information
-
the N-terminal signal peptide of AaTPS2 (46 amino acid residues) before RR motif is truncated and recombinantly expressed in Escherichia coli strain BL21(DE3)
additional information
two TPSs from the Camphor tree Cinnamomum camphora are analyzed, one of these, CiCaMS, acts as a monoterpene synthase (monoTPS), and mediates the production of myrcene (EC 4.2.3.15), while the other, CiCaSSy, acts as a sesquiterpene synthase (sesquiTPS), and catalyses the production of alpha-santalene (EC 4.2.3.82), beta-santalene (EC 4.2.3.83), and trans-alpha-bergamotene (EC 4.2.3.81). These enzymes share 97% DNA sequence identity and differ only in 22 amino acid residues out of 553. To understand which residues are essential for the catalysis of monoterpenes resp. sesquiterpenes, a number of hybrid synthases are prepared, and supplemented by a set of single-residue variants. These are tested for their ability to produce monoterpenes and sesquiterpenes by in vivo production of sesquiterpenes in transgenic Escherichia coli, and by in vitro enzyme assays. Three residues in the sequence can mediate the change in product specificity from a monoterpene synthase to a sesquiterpene synthase. Another set of three residues defines the sesquiterpene product profile, including the ratios between sesquiterpene products. Cloning of CiCaMS/CiCaSSy hybrids and single mutants, overview. Three single amino acid positions are crucial to introduce sesquiTPS activity in CiCaMS: substitutions F294M, L403F and L404V each result in sesquiTPS activity of the monoTPS
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme without N-terminal signal peptide from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
gene CiCaMS, cDNA cloning from root, sequence comparisons and phylogenetic analysis, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) containing an additional plasmid pBbA5c-MevT-MBIS-NPtll expressing all genes necessary for the synthesis of farnesyl diphosphate (FDP). Transient recombinant expression of the enzyme in Nicotiana benthamiana leaves, transformation by Agrobacterium tumefaciens strain AGL0 via electroporation. Transient expression of CiCaMS leads to emission of myrcene
gene TPS2, cloning from a cDNA library, sequence comparisons and phylogenetic analysis and tree, quantitative RT-PCR expression analysis, recombinant expression of His-tagged enzyme without after removing the N-terminal plastid targeting sequence in Escherichia coli strain BL21(DE3)
mutated enzymes are generated using the QuickChange II site-directed mutagenesis kit. The PCR-based mutagenesis protocol is performed using pET200-D-TOPO harbouring the respective AcTPS2 cDNAs as template. The single-site mutant enzymes overexpressed in Escherichia coli.
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AaTPS2 is upregulated after mechanical wounding, but treatments with phytohormones (salicylic acid, methyl jasmonate, and gibberellin) does not affect the expression of AaTPS2
expression correlates well with floral volatile organic compounds emission in scented Alstroemeria genotypes
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bohlmann, J.; Steele C.L.; Croteau, R.
Monoterpene synthases from grand fir (Abies grandis): cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase
J. Biol. Chem.
272
21784-21792
1997
Abies grandis (O24474), Abies grandis
brenda
Bohlmann, J.; Martin, D.; Oldham, N.J.; Gershenzon, J.
Terpenoid secondary metabolism in Arabidopsis thaliana: cDNA cloning, characterization, and functional expression of a myrcene/(E)-beta-ocimene synthase
Arch. Biochem. Biophys.
375
261-269
2000
Arabidopsis thaliana (Q9ZUH4), Arabidopsis thaliana
brenda
Wise, M.L.; Rorrer, G.L.; Polzin, J.J.; Croteau, R.
Biosynthesis of marine natural products: isolation and characterization of a myrcene synthase from cultured tissues of the marine red alga Ochtodes secundiramea
Arch. Biochem. Biophys.
400
125-132
2002
Ochtodes secundiramea
brenda
Hosoi, M.; Ito, M.; Yagura, T.; Adams, R.P.; Honda, G.
cDNA isolation and functional expression of myrcene synthase from Perilla frutescens
Biol. Pharm. Bull.
27
1979-1985
2004
Perilla frutescens
brenda
Green, S.; Squire, C.J.; Nieuwenhuizen, N.J.; Baker, E.N.; Laing, W.
Defining the potassium binding region in an apple terpene synthase
J. Biol. Chem.
284
8661-8669
2009
Actinidia chinensis
brenda
Gilg, A.B.; Tittiger, C.; Blomquist, G.J.
Unique animal prenyltransferase with monoterpene synthase activity
Naturwissenschaften
96
731-735
2009
Ips pini (Q58GE8)
brenda
Aros, D.; Gonzalez, V.; Allemann, R.K.; Mueller, C.T.; Rosati, C.; Rogers, H.J.
Volatile emissions of scented Alstroemeria genotypes are dominated by terpenes, and a myrcene synthase gene is highly expressed in scented Alstroemeria flowers
J. Exp. Bot.
63
2739-2752
2012
Alstroemeria caryophyllaea
brenda
Ruan, J.X.; Li, J.X.; Fang, X.; Wang, L.J.; Hu, W.L.; Chen, X.Y.; Yang, C.Q.
Isolation and characterization of three new monoterpene synthases from Artemisia annua
Front. Plant Sci.
7
638
2016
Artemisia annua (A0A068L9J0), Artemisia annua
brenda
Kim, E.M.; Eom, J.H.; Um, Y.; Kim, Y.; Woo, H.M.
Microbial synthesis of myrcene by metabolically engineered Escherichia coli
J. Agric. Food Chem.
63
4606-4612
2015
Quercus ilex
brenda
Di Girolamo, A.; Durairaj, J.; van Houwelingen, A.; Verstappen, F.; Bosch, D.; Cankar, K.; Bouwmeester, H.; de Ridder, D.; van Dijk, A.D.J.; Beekwilder, J.
The santalene synthase from Cinnamomum camphora reconstruction of a sesquiterpene synthase from a monoterpene synthase
Arch. Biochem. Biophys.
695
108647
2020
Cinnamomum camphora (A0A7S6L0M3)
brenda
Han, J.; Li, T.; Wang, X.; Zhang, X.; Bai, X.; Shao, H.; Wang, S.; Hu, Z.; Wu, J.; Leng, P.
AmMYB24 regulates floral terpenoid biosynthesis induced by blue light in snapdragon flowers
Front. Plant Sci.
13
885168
2022
Antirrhinum majus
brenda
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